Journal
BIOPHYSICAL CHEMISTRY
Volume 143, Issue 1-2, Pages 102-105Publisher
ELSEVIER
DOI: 10.1016/j.bpc.2009.03.007
Keywords
Optical tweezers; Single bond dissociation; Receptor-ligand interaction; Bond strength; Lewis b receptor
Funding
- Magn. Bergvalls Foundation
- Swedish Research Council/VRNT
- Swedish Research Council/VRM
- Umea University Biotechnology Fund
- Cancerfonden
- J.C. Kempe and Seth M. Kempe Memorial Foundation
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The binding strength of the Helicobacter pylori adhesin-receptor complex BabA-ABO/Lewis b has been analyzed by means of dynamic force spectroscopy. High-resolution measurements of rupture forces were performed in situ on single bacterial cells, expressing the high-affinity binding BabA adhesin, by the use of force measuring optical tweezers. The resulting force spectra revealed the mechanical properties of a single BabA-Leb bond. It was found that the bond is dominated by one single energy barrier and that it is a slip-bond. The bond length and thermal off-rate were assessed to be 0.86 +/- 0.07 nm and 0.015 +/- 0.006 s(-1), respectively. (C) 2009 Elsevier B.V. All rights reserved.
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